Aquaporins (AQPs) are membrane proteins serving in the transfer of water and small solutes across cellular membranes. AQPs play a variety of roles in the body such as urine formation, prevention from dehydration in covering epithelia, water handling in the bloodbrain barrier, secretion, conditioning of the sensory system, cell motility and metastasis, formation of cell junctions, and fat metabolism. The kidney plays a central role in water homeostasis in the body. At least seven isoforms, namely AQP1, AQP2, AQP3, AQP4, AQP6, AQP7, and AQP11, are expressed. Among them, AQP2, the anti-diuretic hormone (ADH)-regulated water channel, plays a critical role in water reabsorption. AQP2 is expressed in principal cells of connecting tubules and collecting ducts, where it is stored in Rab11-positive storage vesicles in the basal state. Upon ADH stimulation, AQP2 is translocated to the apical plasma membrane, where it serves in the inXux of water. The translocation process is regulated through the phosphorylation of AQP2 by protein kinase A. As soon as the stimulation is terminated, AQP2 is retrieved to early endosomes, and then transferred back to the Rab 11-positive storage compartment. Some AQP2 is secreted via multivesicular bodies into the urine as exosomes. Actin plays an important role in the intracellular traYcking of AQP2. Recent Wndings have shed light on the molecular basis that controls the traYcking of AQP2.

Aquaporins (AQPs), membrane water channel proteins expressed in various tissues and organs, serve in the transfer of water and small solutes across the membrane. We raised antibodies to AQPs using isoform-specific synthetic peptides and surveyed their expression in the rat nasal olfactory and respiratory mucosae. AQP1, AQP3, AQP4, and AQP5 were detected by immunohistochemical and immunoblotting analyses. AQP1 was expressed in the endothelial cells of blood vessels and the surrounding connective tissue cells in the olfactory and respiratory mucosae. AQP1 may be involved in water transfer across the blood vessel wall. In the olfactory epithelium, no AQP was detected in the olfactory sensory cells. Instead, AQP3 was abundant in the olfactory epithelium, where it was localized in the supporting cells and basal cells. Expression of AQP3 was mostly restricted to the basal cells in the respiratory epithelium. In marked contrast, AQP4 was abundant in the respiratory epithelium, but its abundance was limited to the basal cells in the olfactory epithelium. In the Bowman's gland, AQP5 was localized in the apical membrane in the secretory acinar cells, whereas AQP3 and AQP4 were found in the basolateral membrane. Similar localization was seen in its duct cells. These results showed a distinct localization pattern for AQPs in the olfactory epithelium. AQP3 and AQP4 in the supporting cells and basal cells may play an important role in generating and maintaining the specific microenvironment around the olfactory sensory cells. AQP3, AQP4, and AQP5 in the Bowman's gland may serve in the secretion to generate the microenvironment at the apical surface of the olfactory dendrites for odorant reception.

Water channel aquaporin 5 (AQP5) is present in the apical membrane of the salivary gland acinar cells. We examined changes of AQP5-distribution during the fusion process of secretory granule membranes into the apical membrane and subsequent recovery process in the mouse parotid gland by administering isoproterenol (IPR) in vivo. We performed immunoperoxidase, immunofluorescence and immunoelectron microscopy. In the basal state, AQP5 was localized mainly in the apical membrane of the acinar cell. It was also present in the basolateral membrane to a lesser extent. When IPR was administered to mice, dot-like, vesicle-like and vacuole-like labeling for AQP5 was seen in the subapical regions by light microscopy. By immunoelectron microscopy, AQP5 was localized at both the apical and basolateral plasma membranes in the basal state. At 5 and 30 min after the IPR-administration, acinar lumen became enlarged and small invaginations formed by fusion of secretory granules were seen. AQP5 was positive along the apical plasma membrane and its small invaginations. At 60 min, large invaginations of the lumen were formed. AQP5 remained positive in the membrane of these large invaginations. At 6 h, large invaginations disappeared and AQP5 was localized in the apical plasma membrane. AQP5 was restricted to plasma membranes and continuous invaginations formed by the exocytosis of secretory granules. AQP5 was not detected in the cytoplasm. These observations show that AQP5 does not seem to be endocytosed during the membrane recycling process following the exocytosis.

No abstract